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Integrin beta-1 (Fibronectin receptor subunit beta) (VLA-4 subunit beta) (CD antigen CD29)

 ITB1_MOUSE              Reviewed;         798 AA.
P09055; F6R105; Q3TIW5; Q3TWH6; Q60993; Q61126; Q8BTU0; Q8BVU1;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
07-JUN-2017, entry version 190.
RecName: Full=Integrin beta-1;
AltName: Full=Fibronectin receptor subunit beta;
AltName: Full=VLA-4 subunit beta;
AltName: CD_antigen=CD29;
Flags: Precursor;
Name=Itgb1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
PubMed=3262537; DOI=10.1016/0014-5793(88)80503-9;
Tominaga S.;
"Murine mRNA for the beta-subunit of integrin is increased in BALB/c-
3T3 cells entering the G1 phase from the G0 state.";
FEBS Lett. 238:315-319(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD;
TISSUE=Head, Osteoclast, Placenta, and Thymocyte;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-798 (ISOFORM 1).
STRAIN=BALB/cJ;
PubMed=2523953; DOI=10.1084/jem.169.5.1589;
Holers V.M., Ruff T.G., Parks D.L., McDonald J.A., Ballard L.L.,
Brown E.J.;
"Molecular cloning of a murine fibronectin receptor and its expression
during inflammation. Expression of VLA-5 is increased in activated
peritoneal macrophages in a manner discordant from major
histocompatibility complex class II.";
J. Exp. Med. 169:1589-1605(1989).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 595-798 (ISOFORM 1).
PubMed=2521606; DOI=10.1016/0014-4827(89)90080-3;
Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.;
"Coordinate induction of fibronectin, fibronectin receptor,
tropomyosin, and actin genes in serum-stimulated fibroblasts.";
Exp. Cell Res. 180:537-545(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 718-798 (ISOFORM 2), FUNCTION,
INTERACTION WITH ITGA7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Myoblast;
PubMed=8567725; DOI=10.1083/jcb.132.1.211;
Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D.,
Maier A., Tarone G., Koteliansky V.E., Burridge K.;
"Beta 1D integrin displaces the beta 1A isoform in striated muscles:
localization at junctional structures and signaling potential in
nonmuscle cells.";
J. Cell Biol. 132:211-226(1996).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-798.
TISSUE=Skeletal muscle;
PubMed=8870969;
Baudoin C., Van der Flier A., Borradori L., Sonnenberg A.;
"Genomic organization of the mouse beta 1 gene: conservation of the
beta 1D but not of the beta 1B and beta 1C integrin splice variants.";
Cell Adhes. Commun. 4:1-11(1996).
[10]
DISRUPTION PHENOTYPE.
PubMed=9553049; DOI=10.1101/gad.12.8.1202;
Baudoin C., Goumans M.J., Mummery C., Sonnenberg A.;
"Knockout and knockin of the beta1 exon D define distinct roles for
integrin splice variants in heart function and embryonic
development.";
Genes Dev. 12:1202-1216(1998).
[11]
INTERACTION WITH FBLN5.
PubMed=11805835; DOI=10.1038/415171a;
Nakamura T., Lozano P.R., Ikeda Y., Iwanaga Y., Hinek A.,
Minamisawa S., Cheng C.F., Kobuke K., Dalton N., Takada Y.,
Tashiro K., Ross J., Honjo T., Chien K.R.;
"Fibulin-5/DANCE is essential for elastogenesis in vivo.";
Nature 415:171-175(2002).
[12]
INTERACTION WITH EMP2.
PubMed=12189152; DOI=10.1074/jbc.M206868200;
Wadehra M., Iyer R., Goodglick L., Braun J.;
"The tetraspan protein epithelial membrane protein-2 interacts with
beta1 integrins and regulates adhesion.";
J. Biol. Chem. 277:41094-41100(2002).
[13]
FUNCTION, AND INTERACTION WITH NMRK2.
PubMed=12941630; DOI=10.1016/S0012-1606(03)00304-X;
Li J., Rao H., Burkin D., Kaufman S.J., Wu C.;
"The muscle integrin binding protein (MIBP) interacts with alpha7beta1
integrin and regulates cell adhesion and laminin matrix deposition.";
Dev. Biol. 261:209-219(2003).
[14]
FUNCTION, AND INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
Fukushi J., Makagiansar I.T., Stallcup W.B.;
"NG2 proteoglycan promotes endothelial cell motility and angiogenesis
via engagement of galectin-3 and alpha3beta1 integrin.";
Mol. Biol. Cell 15:3580-3590(2004).
[15]
INTERACTION WITH DAB2.
PubMed=15734730; DOI=10.1074/jbc.M500974200;
Prunier C., Howe P.H.;
"Disabled-2 (Dab2) is required for transforming growth factor beta-
induced epithelial to mesenchymal transition (EMT).";
J. Biol. Chem. 280:17540-17548(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[17]
FUNCTION, AND MUTAGENESIS OF TYR-783 AND TYR-795.
PubMed=18804435; DOI=10.1016/j.devcel.2008.08.001;
Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H.,
Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R.,
Kallio M., Ivaska J.;
"Integrin trafficking regulated by Rab21 is necessary for
cytokinesis.";
Dev. Cell 15:371-385(2008).
[18]
INTERACTION WITH FERMT2.
PubMed=18483218; DOI=10.1101/gad.469408;
Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M.,
Fassler R.;
"Kindlin-2 controls bidirectional signaling of integrins.";
Genes Dev. 22:1325-1330(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363; ASN-366; ASN-376 AND
ASN-669.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[22]
FUNCTION, AND INTERACTION WITH FGR AND HCK.
PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
Berton G.;
"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
migration.";
FEBS Lett. 584:15-21(2010).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21768292; DOI=10.1083/jcb.201007108;
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
fibronectin deposition.";
J. Cell Biol. 194:307-322(2011).
-!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated
sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
fibronectin. Alpha-4/beta-1 recognizes one or more domains within
the alternatively spliced CS-1 and CS-5 regions of fibronectin.
Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor
for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin
alpha-9/beta-1 is a receptor for VCAM1, cytotactin and
osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in
cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin,
thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a
docking site for FAP (seprase) at invadopodia plasma membranes in
a collagen-dependent manner and hence may participate in the
adhesion, formation of invadopodia and matrix degradation
processes, promoting cell invasion. Alpha-3/beta-1 may mediate
with LGALS3 the stimulation by CSPG4 of endothelial cells
migration. Integrin alpha-V/beta-1 is a receptor for vitronectin.
Beta-1 integrins recognize the sequence R-G-D in a wide array of
ligands. When associated with alpha-7/beta-1 integrin, regulates
cell adhesion and laminin matrix deposition. Involved in promoting
endothelial cell motility and angiogenesis. Involved in osteoblast
compaction through the fibronectin fibrillogenesis cell-mediated
matrix assembly process and the formation of mineralized bone
nodules. May be involved in up-regulation of the activity of
kinases such as PKC via binding to KRT1. Together with KRT1 and
RACK1, serves as a platform for SRC activation or inactivation.
Plays a mechanistic adhesive role during telophase, required for
the successful completion of cytokinesis. ITGA4:ITGB1 binds to
fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-
dependent fractalkine signaling (By similarity). ITGA4:ITGB1 and
ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct
from the classical ligand-binding site (site 1) and this induces
integrin conformational changes and enhanced ligand binding to
site 1 (By similarity). ITGA5:ITGB1 acts as a receptor for
fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to
FBN1 (By similarity). {ECO:0000250|UniProtKB:P05556,
ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153,
ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19903482,
ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:8567725}.
-!- FUNCTION: Isoform 2: Isoform 2 displaces isoform 1 in striated
muscles.
-!- SUBUNIT: Interacts with seprase FAP (seprase); the interaction
occurs at the cell surface of invadopodia membrane in a collagen-
dependent manner (By similarity). Heterodimer of an alpha and a
beta subunit. Beta-1 associates with either alpha-1, alpha-2,
alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9,
alpha-10, alpha-11 or alpha-V. Binds LGALS3BP and NMRK2, when
associated with alpha-7, but not with alpha-5. Interacts with
FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the presence
of RACK1 and SRC. Interacts with JAML; integrin alpha-4/beta-1 may
regulate leukocyte to endothelial cells adhesion by controlling
JAML homodimerization. Interacts with RAB21. Interacts (via the
cytoplasmic region) with RAB25 (via the hypervariable C-terminal
region). Interacts with MYO10. Interacts with ITGB1BP1 (via C-
terminal region); the interaction is a prerequisite for focal
adhesion disassembly. Interacts with TLN1; the interaction is
prevented by competitive binding of ITGB1BP1. Interacts with
ACAP1; required for ITGB1 recycling. Interacts with ASAP3.
Interacts with FERMT2; the interaction is inhibited in presence of
ITGB1BP1. Interacts with DAB2. Interacts with FGR and HCK. Isoform
2 interacts with alpha-7A and alpha-7B in adult skeletal muscle.
Isoform 2 interacts with alpha-7B in cardiomyocytes of adult
heart. Interacts with EMP2; the interaction may be direct or
indirect and ITGB1 has an heterodimer form (PubMed:12189152).
ITGA5:ITGB1 interacts with NOV (By similarity). ITGA4:ITGB1 is
found in a ternary complex with CX3CR1 and CX3CL1 (By similarity).
ITGA5:ITGB1 interacts with FBN1 (By similarity).
{ECO:0000250|UniProtKB:P05556, ECO:0000269|PubMed:12189152,
ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153,
ECO:0000269|PubMed:15734730, ECO:0000269|PubMed:18483218,
ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:8567725}.
-!- INTERACTION:
P26955:Csf2rb; NbExp=2; IntAct=EBI-644224, EBI-1810026;
Q01768:Nme2; NbExp=3; IntAct=EBI-644224, EBI-642573;
Q6F5E0:Tmem158; NbExp=3; IntAct=EBI-644224, EBI-645317;
Q91YD9:Wasl; NbExp=2; IntAct=EBI-644224, EBI-642417;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, invadopodium membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Recycling endosome
{ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:8567725}.
Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection,
lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection,
ruffle {ECO:0000250|UniProtKB:P05556}. Cell junction, focal
adhesion {ECO:0000250|UniProtKB:P05556}. Cell surface
{ECO:0000250|UniProtKB:P05556}. Note=Colocalizes with ITGB1BP1 and
metastatic suppressor protein NME2 at the edge or peripheral
ruffles and lamellipodia during the early stages of cell spreading
on fibronectin or collagen. Translocates from peripheral focal
adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner.
Enriched preferentially at invadopodia, cell membrane protrusions
that correspond to sites of cell invasion, in a collagen-dependent
manner. Localized at plasma and ruffle membranes in a collagen-
independent manner. {ECO:0000250|UniProtKB:P05556}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane, sarcolemma. Cell
junction. Note=In cardiac muscle, isoform 2 is found in costameres
and intercalated disks.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Beta-1A;
IsoId=P09055-1; Sequence=Displayed;
Name=2; Synonyms=Beta-1D;
IsoId=P09055-2; Sequence=VSP_053581, VSP_053582;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in skeletal and cardiac
muscles only (at protein level). Isoform 1 is very weakly
expressed in striated muscles and not detected in adult skeletal
muscle fibers and cardiomyocytes. {ECO:0000269|PubMed:8567725}.
-!- DEVELOPMENTAL STAGE: Isoform 2 is not detected in proliferating
myoblasts, but it appears immediately after myoblast fusion and
its amount continues to rise during myotube growth and maturation
reaching its highest level at day 9 through day 10, when mature
differentiated myotubes appear in cell culture. Isoform 1
expression is down-regulated during myodifferentiation in culture
and it is completely displaced by isoform 2 in mature
differentiated myotubes. {ECO:0000269|PubMed:8567725}.
-!- PTM: The cysteine residues are involved in intrachain disulfide
bonds. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Isoform 2 knockout mice are viable and
fertile, but male mice display a mild abnormality of cardiac
function reflected by an increased expression of atrial
natriuretic peptide and beta myosin heavy chain. Muscles do not
show any histological or ultrastructural alterations. Replacement
of isoform 1 by isoform 2 results in embryonic lethality before
16.5 dpc with a plethora of developmental defects including open
neural tube, which is abnormally waved both rostrally and
caudally. Some embryos lack part of the hindbrain and in most
embryos the first branchial arch is shortened, which in some of
the embryos leaves the tongue exposed. Abnormally strong
fibronectin staining is seen in the mesenchyme under the open
neural tube. Extravasation of red blood cells is evident in
various tissues and they are also found in the pericardial cavity.
Choroid plexus is virtually absent correlating with the presence
of an abnormally smooth head and small brain cavities. At later
developmental stages, a striking feature is the lack of a lower
jaw and a dysmorphic lower face. These defects are in part caused
by the abnormal migration of neuroepithelial cells.
{ECO:0000269|PubMed:9553049}.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC36379.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; Y00769; CAA68738.1; -; mRNA.
EMBL; AK076526; BAC36379.1; ALT_INIT; mRNA.
EMBL; AK088729; BAC40532.1; -; mRNA.
EMBL; AK159689; BAE35290.1; -; mRNA.
EMBL; AK167682; BAE39731.1; -; mRNA.
EMBL; AC156608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466525; EDL11832.1; -; Genomic_DNA.
EMBL; BC050906; AAH50906.1; -; mRNA.
EMBL; X15202; CAA33272.1; -; mRNA.
EMBL; U37029; AAA80243.1; -; mRNA.
EMBL; U47283; AAA88821.1; -; Genomic_DNA.
CCDS; CCDS22791.1; -. [P09055-1]
PIR; PL0104; IJMSFB.
PIR; S01659; S01659.
RefSeq; NP_034708.1; NM_010578.2. [P09055-1]
UniGene; Mm.263396; -.
ProteinModelPortal; P09055; -.
SMR; P09055; -.
BioGrid; 200826; 49.
DIP; DIP-46247N; -.
IntAct; P09055; 60.
MINT; MINT-1573412; -.
STRING; 10090.ENSMUSP00000087457; -.
iPTMnet; P09055; -.
PhosphoSitePlus; P09055; -.
SwissPalm; P09055; -.
EPD; P09055; -.
MaxQB; P09055; -.
PaxDb; P09055; -.
PeptideAtlas; P09055; -.
PRIDE; P09055; -.
Ensembl; ENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809. [P09055-1]
GeneID; 16412; -.
KEGG; mmu:16412; -.
UCSC; uc009nzv.2; mouse. [P09055-1]
CTD; 3688; -.
MGI; MGI:96610; Itgb1.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
GeneTree; ENSGT00760000119064; -.
HOGENOM; HOG000252936; -.
HOVERGEN; HBG006190; -.
InParanoid; P09055; -.
KO; K05719; -.
OMA; FFDEDDC; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; P09055; -.
TreeFam; TF105392; -.
Reactome; R-MMU-1566948; Elastic fibre formation.
Reactome; R-MMU-1566977; Fibronectin matrix formation.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-210991; Basigin interactions.
Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
Reactome; R-MMU-216083; Integrin cell surface interactions.
Reactome; R-MMU-3000157; Laminin interactions.
Reactome; R-MMU-3000170; Syndecan interactions.
Reactome; R-MMU-3000178; ECM proteoglycans.
Reactome; R-MMU-416700; Other semaphorin interactions.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
Reactome; R-MMU-447041; CHL1 interactions.
Reactome; R-MMU-8874081; MET activates PTK2 signaling.
Reactome; R-MMU-8875513; MET interacts with TNS proteins.
ChiTaRS; Itgb1; mouse.
PRO; PR:P09055; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000025809; -.
CleanEx; MM_ITGB1; -.
ExpressionAtlas; P09055; baseline and differential.
Genevisible; P09055; MM.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0043197; C:dendritic spine; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0030175; C:filopodium; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0034665; C:integrin alpha1-beta1 complex; ISO:MGI.
GO; GO:0034680; C:integrin alpha10-beta1 complex; ISO:MGI.
GO; GO:0034681; C:integrin alpha11-beta1 complex; ISO:MGI.
GO; GO:0034666; C:integrin alpha2-beta1 complex; ISO:MGI.
GO; GO:0034667; C:integrin alpha3-beta1 complex; ISO:MGI.
GO; GO:0034677; C:integrin alpha7-beta1 complex; IDA:MGI.
GO; GO:0014704; C:intercalated disc; IDA:MGI.
GO; GO:0071438; C:invadopodium membrane; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0035748; C:myelin sheath abaxonal region; IDA:BHF-UCL.
GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0097060; C:synaptic membrane; IDA:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0019960; F:C-X3-C chemokine binding; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:MGI.
GO; GO:0001968; F:fibronectin binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; IPI:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0032403; F:protein complex binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0048675; P:axon extension; IMP:MGI.
GO; GO:0071711; P:basement membrane organization; IMP:CAFA.
GO; GO:0007161; P:calcium-independent cell-matrix adhesion; ISO:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0001708; P:cell fate specification; IMP:MGI.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:MGI.
GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0021943; P:formation of radial glial scaffolds; IMP:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:0008354; P:germ cell migration; IMP:MGI.
GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:MGI.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
GO; GO:0045214; P:sarcomere organization; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR027071; Integrin_beta-1.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom.
InterPro; IPR016201; PSI.
InterPro; IPR002035; VWF_A.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF53; PTHR10082:SF53; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS00243; INTEGRIN_BETA; 3.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome; Disulfide bond;
Endosome; Glycoprotein; Integrin; Isopeptide bond; Magnesium;
Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 20
CHAIN 21 798 Integrin beta-1.
/FTId=PRO_0000016335.
TOPO_DOM 21 728 Extracellular. {ECO:0000255}.
TRANSMEM 729 751 Helical. {ECO:0000255}.
TOPO_DOM 752 798 Cytoplasmic. {ECO:0000255}.
DOMAIN 140 378 VWFA.
REPEAT 466 515 I.
REPEAT 516 559 II.
REPEAT 560 598 III.
REPEAT 599 635 IV.
REGION 207 213 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05556}.
REGION 295 314 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05556}.
REGION 466 635 Cysteine-rich tandem repeats.
REGION 762 767 Signal for sorting from recycling
endosomes; interaction with ACAP1.
{ECO:0000250}.
REGION 785 792 Interaction with ITGB1BP1. {ECO:0000250}.
METAL 152 152 Magnesium. {ECO:0000250}.
METAL 154 154 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 156 156 Calcium 1. {ECO:0000250}.
METAL 157 157 Calcium 1. {ECO:0000250}.
METAL 189 189 Calcium 2. {ECO:0000250}.
METAL 244 244 Calcium 2. {ECO:0000250}.
METAL 246 246 Calcium 2. {ECO:0000250}.
METAL 248 248 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 249 249 Calcium 2. {ECO:0000250}.
METAL 249 249 Magnesium. {ECO:0000250}.
MOD_RES 777 777 Phosphothreonine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 783 783 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 789 789 Phosphothreonine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 794 794 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05556}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19656770}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19656770}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
DISULFID 27 45 {ECO:0000250}.
DISULFID 35 464 {ECO:0000250}.
DISULFID 38 75 {ECO:0000250}.
DISULFID 48 64 {ECO:0000250}.
DISULFID 207 213 {ECO:0000250}.
DISULFID 261 301 {ECO:0000250}.
DISULFID 401 415 {ECO:0000250}.
DISULFID 435 462 {ECO:0000250}.
DISULFID 466 691 {ECO:0000250}.
DISULFID 477 489 {ECO:0000250}.
DISULFID 486 525 {ECO:0000250}.
DISULFID 491 500 {ECO:0000250}.
DISULFID 502 516 {ECO:0000250}.
DISULFID 531 536 {ECO:0000250}.
DISULFID 533 568 {ECO:0000250}.
DISULFID 538 553 {ECO:0000250}.
DISULFID 555 560 {ECO:0000250}.
DISULFID 574 579 {ECO:0000250}.
DISULFID 576 607 {ECO:0000250}.
DISULFID 581 590 {ECO:0000250}.
DISULFID 592 599 {ECO:0000250}.
DISULFID 613 618 {ECO:0000250}.
DISULFID 615 661 {ECO:0000250}.
DISULFID 620 630 {ECO:0000250}.
DISULFID 633 636 {ECO:0000250}.
DISULFID 640 649 {ECO:0000250}.
DISULFID 646 723 {ECO:0000250}.
DISULFID 665 699 {ECO:0000250}.
CROSSLNK 794 794 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P05556}.
VAR_SEQ 778 778 G -> Q (in isoform 2).
{ECO:0000303|PubMed:8567725}.
/FTId=VSP_053581.
VAR_SEQ 786 798 AVTTVVNPKYEGK -> PINNFKNPNYGRKAGL (in
isoform 2). {ECO:0000303|PubMed:8567725}.
/FTId=VSP_053582.
MUTAGEN 783 783 Y->F: Reduced endocytosis; when
associated with F-795.
{ECO:0000269|PubMed:18804435}.
MUTAGEN 795 795 Y->F: Reduced endocytosis; when
associated with F-783.
{ECO:0000269|PubMed:18804435}.
CONFLICT 5 5 L -> Q (in Ref. 2; BAC40532).
{ECO:0000305}.
CONFLICT 72 72 K -> E (in Ref. 2; BAE35290).
{ECO:0000305}.
CONFLICT 385 385 E -> D (in Ref. 2; BAC36379).
{ECO:0000305}.
CONFLICT 385 385 E -> P (in Ref. 6; CAA33272).
{ECO:0000305}.
CONFLICT 392 392 G -> A (in Ref. 6; CAA33272).
{ECO:0000305}.
CONFLICT 407 407 G -> E (in Ref. 2; BAC36379).
{ECO:0000305}.
CONFLICT 443 445 IKI -> HSKL (in Ref. 6; CAA33272).
{ECO:0000305}.
SEQUENCE 798 AA; 88231 MW; 26788F7F0A168B56 CRC64;
MNLQLVSWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN TTFLQEGMPT
SARCDDLEAL KKKGCQPSDI ENPRGSQTIK KNKNVTNRSK GMAEKLRPED ITQIQPQQLL
LKLRSGEPQK FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TANKCPNKES ETIKIKPLGF TEEVEVVLQF ICKCNCQSHG IPASPKCHEG
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCRCRVCE CYPNYTGSAC DCSLDTGPCL
ASNGQICNGR GICECGACKC TDPKFQGPTC ETCQTCLGVC AEHKECVQCR AFNKGEKKDT
CAQECSHFNL TKVESREKLP QPVQVDPVTH CKEKDIDDCW FYFTYSVNGN NEAIVHVVET
PDCPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK


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